Evidence map›Paper›PMID 23509279›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Catalytic DNA with phosphatase activity.

Jagadeeswaran Chandrasekar, Scott K Silverman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024
    Article
  3. DNA Catalysis: Design, Function, and Optimization.Molecules (Basel, Switzerland) · 2024
    Review
  4. Construction and Application of DNAzyme-based Nanodevices.Chemical research in Chinese universities · 2023
    Review
  5. Pushing the Limits of Nucleic Acid Function.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Review
  6. Supernova: A Deoxyribozyme that Catalyzes a Chemiluminescent Reaction.Angewandte Chemie (International ed. in English) · 2022
    Article
  7. Solution NMR Spectroscopy as a Tool to Study DNAzyme Structure and Function.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Biosensing with DNAzymes.Chemical Society reviews · 2021
    Review
  9. Article
  10. Article
  11. DNAmoreDB, a database of DNAzymes.Nucleic acids research · 2021
    Article
  12. DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021
    Article
  13. Nucleic Acids Analysis.Science China. Chemistry · 2021
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. DNA-catalyzed glycosylation using aryl glycoside donors.Chemical communications (Cambridge, England) · 2016
    Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jagadeeswaran ChandrasekarDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Scott K Silverman
University of Illinois Urbana-Champaign · US

Funding

Deoxyribozymes that ligate RNAR01GM065966 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI SILVERMAN, SCOTT K · 2003 to 2016
$4.2M
NIGMS NIH HHS R01 GM065966NIGMS NIH HHS R01GM065966
6 · The paper itself

Abstract

Catalytic DNA sequences (deoxyribozymes, DNA enzymes, or DNAzymes) have been identified by in vitro selection for various catalytic activities. Expanding the limits of DNA catalysis is an important fundamental objective and may facilitate practical utility of catalysts that can be obtained from entirely unbiased (random) sequence populations. In this study, we show that DNA can catalyze Zn(2+)-dependent phosphomonoester hydrolysis of tyrosine and serine side chains (i.e., exhibit phosphatase activity). The best deoxyribozyme decreases the half-life for phosphoserine hydrolysis from as high as >10(10) y to <1 h. The phosphatase activity also occurs with nonpeptidic substrates but with reduced efficiency, indicating a preference for phosphopeptides. The newly identified deoxyribozymes can function with multiple turnover using free peptide substrates, have activity in the presence of human cell lysate or BSA, and catalyze dephosphorylation of a larger protein substrate, suggesting broader application of DNA catalysts as artificial phosphatases.

Indexed as

CatalysisChromatography, High Pressure LiquidDNA, CatalyticElectrophoresis, Polyacrylamide GelHalf-LifeHumansHydrolysisIn Vitro TechniquesMass SpectrometryOligonucleotidesPhosphoric Monoester HydrolasesPhosphorylationPhosphoserinePhosphotyrosineRosaniline DyesDNA, Catalyticmalachite greenOligonucleotidesPhosphoric Monoester HydrolasesPhosphoserinePhosphotyrosineRosaniline Dyes

Identifiers

PMID23509279
PMCPMC3619321
OpenAlexW2004141462

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.